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Literature DB >> 170912

A kinetic method to establish the specificity of spin labelling of macromolecules.

Abstract

A method has been devised for establishing the specificity of spin labelling of a macromolecule. Analysis of the rate of incorporation of spin label under different conditions permits the assignment of reacting groups to classes of differing reactivity. The method is illustrated for the enzyme glycogen phosphorylase b.

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Year: 1975 PMID： 170912 PMCID： PMC1165489 DOI： 10.1042/bj1470609

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

8 in total

1. Protein measurement with the Folin phenol reagent.

Authors: O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal: J Biol Chem Date: 1951-11 Impact factor: 5.157

2. Studies on the interaction of ligands with phosphorylase b using a spin-label probe.

Authors: I D Campbell; R A Dwek; N C Price; G K Radda
Journal: Eur J Biochem Date: 1972-10

3. Improvement of the spin-labelling technique by the use of a radioactive spin label.

Authors: N C Price
Journal: FEBS Lett Date: 1973-11-01 Impact factor: 4.124

4. Probes for the conformational transitions of phosphorylase b. Effect of ligands studied by proton relaxation enhancement, fluorescence and chemical reactivities.

Authors: D J Birkett; R A Dwek; G K Radda; R E Richards; A G Salmon
Journal: Eur J Biochem Date: 1971-06-29

1 in total

1. Properties of matrix-bound dimer and monomer derivatives of immobilized creatine kinase from rabbit skeletal muscle.

Authors: G F Bickerstaff; N C Price
Journal: Biochem J Date: 1978-07-01 Impact factor: 3.857

1 in total

A kinetic method to establish the specificity of spin labelling of macromolecules.

1. Protein measurement with the Folin phenol reagent.

2. Studies on the interaction of ligands with phosphorylase b using a spin-label probe.

3. Improvement of the spin-labelling technique by the use of a radioactive spin label.

4. Probes for the conformational transitions of phosphorylase b. Effect of ligands studied by proton relaxation enhancement, fluorescence and chemical reactivities.

5. The sulfhydryl groups of muscle phosphorylase. V. The reactive sulfhydryl peptides.

6. The reactivity of group-specific chromophoric reagents.

7. The reactivity of thiol groups in aldolase.

8. Magnetic resonance studies of spin-labeled creatine kinase system and interaction of two paramagnetic probes.

1. Properties of matrix-bound dimer and monomer derivatives of immobilized creatine kinase from rabbit skeletal muscle.